title: A folding pathway-dependent score to recognize membrane proteins.
abstract: While various approaches exist to study protein localization, it is still a challenge to predict where proteins localize. Here, we consider a mechanistic viewpoint for membrane localization. Taking into account the steps for the folding pathway of α-helical membrane proteins and relating biophysical parameters to each of these steps, we create a score capable of predicting the propensity for membrane localization and call it FP(3)mem. This score is driven from the principal component analysis (PCA) of the biophysical parameters related to membrane localization. FP(3)mem allows us to rationalize the colocalization of a number of channel proteins with the Cav1.2 channel by their fewer propensities for membrane localization.
authors.affiliation: Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
authors.forename: Hamid
authors.initials: H
authors.lastname: Hadi-Alijanvand
authors.forename: Maryam
authors.initials: M
authors.lastname: Rouhani
authors.forename: Elizabeth A
authors.initials: EA
authors.lastname: Proctor
authors.forename: Nikolay V
authors.initials: NV
authors.lastname: Dokholyan
authors.forename: Ali A
authors.initials: AA
authors.lastname: Moosavi-Movahedi
mesh_terms: D000818:Animals; D015220:Calcium Channels; D030562:Databases, Protein; D005057:Eukaryotic Cells / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D011387:Prokaryotic Cells / Q000378:metabolism; D017510:Protein Folding; D017433:Protein Structure, Secondary; D021381:Protein Transport; D018091:Receptors, AMPA / Q000378:metabolism; D016194:Receptors, N-Methyl-D-Aspartate / Q000378:metabolism
chemical_list: D015220:Calcium Channels; D008565:Membrane Proteins; D018091:Receptors, AMPA; D016194:Receptors, N-Methyl-D-Aspartate